Evidence map›Paper›PMID 33020946›Full record

ArticleProtein science : a publication of the Protein Society2020

Kinetic characterization and structure analysis of an altered polyol dehydrogenase with d-lactate dehydrogenase activity.

Diane Chauliac, Qingzhao Wang, Franz J St John, Grace Jones, Jason C Hurlbert, Lonnie O Ingram, Keelnatham T Shanmugam

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 45% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Microbial adaptive evolution.Journal of industrial microbiology & biotechnology · 2022
    Review
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Diane ChauliacDepartment of Microbiology and Cell Science, University of Florida, Gainesville, Florida, USA.
Qingzhao WangDepartment of Microbiology and Cell Science, University of Florida, Gainesville, Florida, USA.
Franz J St JohnForest Products Laboratory, USDA Forest Service, Madison, Wisconsin, USA.ORCID 0000-0003-3458-5628
Grace JonesDepartment of Chemistry, Physics and Geology, Winthrop University, Rock Hill, South Carolina, USA.
Jason C HurlbertDepartment of Chemistry, Physics and Geology, Winthrop University, Rock Hill, South Carolina, USA.
Lonnie O IngramDepartment of Microbiology and Cell Science, University of Florida, Gainesville, Florida, USA.
Keelnatham T ShanmugamDepartment of Microbiology and Cell Science, University of Florida, Gainesville, Florida, USA.
University of Florida · USWinthrop University · USForest Products Laboratory · US

Funding

Supplement for South Carolina BRIN - 1P20 RR16461P20RR016461 · NCRR · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI DEAVOR, JAMES · 2001 to 2011
$32.3M
NCRR NIH HHS 5 P20 RR016461NCRR NIH HHS P20 RR016461
6 · The paper itself

Abstract

During adaptive metabolic evolution a native glycerol dehydrogenase (GDH) acquired a d-lactate dehydrogenase (LDH) activity. Two active-site amino acid changes were detected in the altered protein. Biochemical studies along with comparative structure analysis using an X-ray crystallographic structure model of the protein with the two different amino acids allowed prediction of pyruvate binding into the active site. We propose that the F245S alteration increased the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 γ-O and the C1 carboxylate of pyruvate. To our knowledge, this is the first GDH to gain LDH activity due to an active site amino acid change, a desired result of in vivo enzyme evolution.

Indexed as

BacillusBacterial ProteinsLactate DehydrogenasesL-Iditol 2-DehydrogenaseBinding SitesCrystallography, X-RayKineticsMutagenesis, Site-DirectedBacterial ProteinsD-lactate dehydrogenaseLactate DehydrogenasesL-Iditol 2-DehydrogenaseBacillus coagulansdirected evolutiond-lactic acidglycerol dehydrogenaselactate dehydrogenase

Identifiers

PMID33020946
PMCPMC7679959
OpenAlexW3091206477

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.